2D68

Structure of the N-terminal domain of FOP (FGFR1OP) protein

2D68 の概要

• エントリーDOI: 10.2210/pdb2d68/pdb
• 分子名称: FOP (2 entities in total)
• 機能のキーワード: alpha helical bundle, dimer, cell cycle
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton, centrosome: O95684
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18309.01

構造登録者

Mikolajka, A. (登録日: 2005-11-10, 公開日: 2006-05-16, 最終更新日: 2024-03-13)

主引用文献

Mikolajka, A.,Yan, X.,Popowicz, G.M.,Smialowski, P.,Nigg, E.A.,Holak, T.A.
Structure of the N-terminal Domain of the FOP (FGFR1OP) Protein and Implications for its Dimerization and Centrosomal Localization.
J.Mol.Biol., 359:863-875, 2006

PubMed Abstract: The fibroblast growth factor receptor 1 (FGFR1) oncogene partner, FOP, is a centrosomal protein that is involved in the anchoring of microtubules (MTS) to subcellular structures. The protein was originally discovered as a fusion partner with FGFR1 in oncoproteins that give rise to stem cell myeloproliferative disorders. A subsequent proteomics screen identified FOP as a component of the centrosome. FOP contains a Lis-homology (LisH) motif found in more than 100 eukaryotic proteins. LisH motifs are believed to be involved in microtubule dynamics and organization, cell migration, and chromosome segregation; several of them are associated with genetic diseases. We report here a 1.6A resolution crystal structure of the N-terminal dimerization domain of FOP. The structure comprises an alpha-helical bundle composed of two antiparallel chains, each of them having five alpha-helices. The central part of the dimer contains the LisH domain. We further determined that the FOP LisH domain is part of a longer N-terminal segment that is required, albeit not sufficient, for dimerization and centrosomal localization of FOP.

PubMed: 16690081
DOI: 10.1016/j.jmb.2006.03.070

実験手法

X-RAY DIFFRACTION (1.6 Å)